ID   MIH_PROBO               Reviewed;          74 AA.
AC   Q10987;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Molt-inhibiting hormone;
DE            Short=MIH;
DE   Flags: Precursor; Fragment;
OS   Procambarus bouvieri (Mexican crayfish).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC   Astacoidea; Cambaridae; Procambarus.
OX   NCBI_TaxID=6729;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eyestalk;
RA   Aguilar-Gaytan R., Cerbon M.A., Cevallos M.A., Huberman A.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-72, PYROGLUTAMATE FORMATION AT GLN-1, AMIDATION AT
RP   VAL-72, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Sinus gland;
RX   PubMed=8735961; DOI=10.1016/0196-9781(96)00010-1;
RA   Aguilar M.B., Falchetto R., Shabanowitz J., Hunt D.F., Huberman A.;
RT   "Complete primary structure of the molt-inhibiting hormone (MIH) of the
RT   Mexican crayfish Procambarus bouvieri (Ortmann).";
RL   Peptides 17:367-374(1996).
CC   -!- FUNCTION: Inhibits Y-organs where molting hormone (ecdysteroid) is
CC       secreted. A molting cycle is initiated when MIH secretion diminishes or
CC       stops (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=8320; Mass_error=3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8735961};
CC   -!- SIMILARITY: Belongs to the arthropod CHH/MIH/GIH/VIH hormone family.
CC       {ECO:0000305}.
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DR   EMBL; U79764; AAB53371.1; -; mRNA.
DR   AlphaFoldDB; Q10987; -.
DR   SMR; Q10987; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.2010.10; -; 1.
DR   InterPro; IPR018251; Crust_neurhormone_CS.
DR   InterPro; IPR031098; Crust_neurohorm.
DR   InterPro; IPR035957; Crust_neurohorm_sf.
DR   InterPro; IPR001166; Hyperglycemic.
DR   InterPro; IPR000346; Hyperglycemic1.
DR   PANTHER; PTHR35981; PTHR35981; 1.
DR   Pfam; PF01147; Crust_neurohorm; 1.
DR   PRINTS; PR00548; HYPRGLYCEMC1.
DR   PRINTS; PR00550; HYPRGLYCEMIC.
DR   SUPFAM; SSF81778; SSF81778; 1.
DR   PROSITE; PS01250; CHH_MIH_GIH; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Hormone;
KW   Neuropeptide; Pyrrolidone carboxylic acid; Secreted.
FT   PEPTIDE         1..72
FT                   /note="Molt-inhibiting hormone"
FT                   /id="PRO_0000019082"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8735961"
FT   MOD_RES         72
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:8735961"
FT   DISULFID        7..43
FT                   /evidence="ECO:0000269|PubMed:8735961"
FT   DISULFID        23..39
FT                   /evidence="ECO:0000269|PubMed:8735961"
FT   DISULFID        26..52
FT                   /evidence="ECO:0000269|PubMed:8735961"
FT   NON_TER         1
SQ   SEQUENCE   74 AA;  8530 MW;  0CFDD183433F847F CRC64;
     QVFDQACKGI YDRAIFKKLE LVCDDCYNLY RKPKVATTCR ENCYANSVFR QCLDDLLLIN
     VVDEYISGVQ IVGK